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Related Concept Videos

MALDI-TOF Mass Spectrometry01:19

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Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...
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Related Experiment Video

Updated: Mar 6, 2026

Detection of Functional Matrix Metalloproteinases by Zymography
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Time-Resolved Analysis of Matrix Metalloproteinase Substrates in Complex Samples.

Pascal Schlage1, Fabian E Egli1, Ulrich Auf dem Keller2

  • 1ETH Zurich, Department of Biology, Institute of Molecular Health Sciences, Otto-Stern-Weg 7, 8093, Zurich, Switzerland.

Methods in Molecular Biology (Clifton, N.J.)
|March 17, 2017
PubMed
Summary

Identifying matrix metalloproteinase (MMP) substrates is crucial for understanding their roles in health and disease. This study presents a time-resolved iTRAQ-TAILS method for MMP substrate discovery in cell cultures, alongside automated data analysis.

Keywords:
ProteaseProteomicsSubstrate discoveryTime-resolved degradomicsiTRAQ-TAILS

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Area of Science:

  • Biochemistry
  • Proteomics
  • Molecular Biology

Background:

  • Matrix metalloproteinases (MMPs) have diverse functions in biological processes and disease pathogenesis.
  • Identifying MMP physiological substrates is essential for understanding their roles.
  • Quantitative mass spectrometry and multiplexing techniques have advanced protease substrate discovery.

Purpose of the Study:

  • To provide a detailed protocol for time-resolved iTRAQ-based Terminal Amine Isotopic Labeling of Substrates (TAILS).
  • To focus on MMP substrate identification and characterization in cell culture supernatants.
  • To introduce an automated procedure for interpreting complex time-resolved iTRAQ-TAILS datasets.

Main Methods:

  • Quantitative mass spectrometry-based proteomics.
  • Terminal Amine Isotopic Labeling of Substrates (TAILS) assay.
  • Isobaric Tandem Mass Tags (iTRAQ) labeling for multiplexing.
  • Time-resolved experimental design.
  • Automated data interpretation pipeline.

Main Results:

  • A robust protocol for time-resolved iTRAQ-TAILS was established for MMP substrate analysis.
  • The method enables identification and characterization of MMP substrates in cell culture supernatants.
  • An automated procedure facilitates efficient interpretation of complex proteomic datasets.

Conclusions:

  • Time-resolved iTRAQ-TAILS is a powerful approach for MMP substrate discovery.
  • This methodology enhances the understanding of MMP functions in biological systems.
  • Automated data analysis streamlines the interpretation of complex proteomic data, accelerating research.